Q9UBU9 (NXF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear RNA export factor 1

Alternative name(s):
Tip-associated protein
Tip-associating protein
mRNA export factor TAP

Gene names

Name:	NXF1
Synonyms:	TAP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	619 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5. Ref.9 Ref.19
Subunit structure	Heterodimer with NXT1. Interacts (via NTF2 domain) with NXT1. The formation of NXF1/NXT1 heterodimers is required for the NXF1-mediated nuclear mRNA export. Interacts with NXT2, E1B-AP5, RAE1, ALYREF/THOC4 and with several nucleoporins. Is part of the exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A, SRRM1, NXF1, UPF1, UPF2, UPF3A, UPF3B, ALYREF/THOC4 and/or REFBP2. Found in a mRNA complex with RENT3A and RENT3B. Interacts with FYTTD1/UIF, EIF4A3, NUPL2 and THOC5. Interacts with Saimiriine herpesvirus 2 TIP protein. Interacts with human herpes virus 1 (HHV-1) ICP27 protein; this interaction allows efficient export of HHV-1 early and late transcripts. Ref.8 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.24
Subcellular location	Nucleus › nucleoplasm. Nucleus speckle. Cytoplasm. Note: Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Ref.20
Tissue specificity	Expressed ubiquitously.
Domain	The minimal CTE binding domain consists of an RNP-type RNA binding domain (RBD) and leucine-rich repeats. Ref.24 The nucleoporin binding domain consists of a NTF2 domain (also called NTF2-like domain) and a TAP-C domain (also called UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2 and the other in the TAP-C domain) which contribute to nucleoporin association and act synergistically to export cellular mRNAs. Ref.24 The NTF2 domain is functional only in the presence of NXT1 and is essential for the export of mRNA from the nucleus. Ref.24 The TAP-C domain mediates direct interactions with nucleoporin-FG-repeats and is necessary and sufficient for localization of NXF1 to the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has a critical role in the interaction with nucleoporins. Ref.24 The leucine-rich repeats are essential for the export of mRNA from the nucleus. Ref.24 The RNA-binding domain is a non-canonical RNP-type domain. Ref.24
Sequence similarities	Belongs to the NXF family. Contains 4 LRR (leucine-rich) repeats. Contains 1 NTF2 domain. Contains 1 RRM (RNA recognition motif) domain. Contains 1 TAP-C domain.

Ontologies

Keywords
Biological process	Host-virus interaction Transport mRNA transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat
Ligand	RNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gene expression Traceable author statement. Source: Reactome mRNA export from nucleus Inferred from direct assay Ref.19. Source: UniProtKB poly(A)+ mRNA export from nucleus Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear inclusion body Inferred from electronic annotation. Source: Compara nuclear pore Inferred from electronic annotation. Source: Compara nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	mRNA binding Inferred from electronic annotation. Source: Compara nucleocytoplasmic transporter activity Inferred from electronic annotation. Source: Compara nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P22575	6	EBI-398874,EBI-866709	From a different organism.
DDX3X	O00571	5	EBI-398874,EBI-353779
DHX9	Q08211	8	EBI-398874,EBI-352022
NXT1	Q9UKK6	2	EBI-398874,EBI-301889
SRSF1	Q07955	5	EBI-398874,EBI-398920
THRAP3	Q9Y2W1	4	EBI-398874,EBI-352039

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UBU9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UBU9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     339-356: SAIRERFPKLLRLDGHEL → RSVVACVSPPGDLHPLGG
     357-619: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 619

619

Nuclear RNA export factor 1

PRO_0000220529

Regions

Domain

119 – 198

80

RRM

Repeat

266 – 291

26

LRR 1

Repeat

292 – 315

24

LRR 2

Repeat

316 – 343

28

LRR 3

Repeat

344 – 371

28

LRR 4

Domain

386 – 536

151

NTF2

Domain

565 – 619

55

TAP-C

Region

1 – 371

371

Interaction with ALYREF/THOC4

Motif

67 – 100

34

Nuclear localization signal

Motif

83 – 110

28

Nuclear export signal

Compositional bias

551 – 561

11

Pro-rich

Natural variations

Alternative sequence

339 – 356

18

SAIRE…DGHEL → RSVVACVSPPGDLHPLGG in isoform 2.

VSP_041427

Alternative sequence

357 – 619

263

Missing in isoform 2.

VSP_041428

Experimental info

Mutagenesis

306 – 308

3

ERE → AAA: Decreases the export of mRNAs from the nucleus.

Mutagenesis

383

1

L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-386. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-386 and A-594. Ref.24

Mutagenesis

386

1

L → R: Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-383. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and A-594. Ref.24

Mutagenesis

399

1

D → A: 60% reduction in mRNA export activity. Ref.24

Mutagenesis

482

1

D → R: 90% reduction in mRNA export activity. Ref.24

Mutagenesis

518

1

I → R: 98% reduction in mRNA export activity. Ref.24

Mutagenesis

521

1

P → Q: 35% reduction in mRNA export activity. Ref.24

Mutagenesis

594

1

W → A: Suppresses FG-nucleoporin binding. Diminishes nuclear rim staining and 88% reduction in mRNA export activity. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and R-386. Ref.24

Mutagenesis

595

1

D → R: Suppresses FG-nucleoporin binding.

Mutagenesis

617

1

F → A: Suppresses FG-nucleoporin binding. Ref.26

Sequence conflict

119

1

W → C in AAB81111. Ref.8

Sequence conflict

256

1

T → N in AAD20016. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

619

Helix Strand Turn

Details...

Beta strand

120 – 124

5

Helix

127 – 129

3

Helix

132 – 141

10

Beta strand

143 – 145

3

Beta strand

150 – 155

6

Beta strand

158 – 164

7

Helix

166 – 174

9

Turn

176 – 178

3

Beta strand

190 – 193

4

Helix

198 – 201

4

Helix

206 – 218

13

Turn

222 – 225

4

Beta strand

226 – 228

3

Helix

232 – 234

3

Helix

236 – 240

5

Helix

250 – 263

14

Beta strand

269 – 271

3

Helix

281 – 285

5

Helix

286 – 289

4

Beta strand

295 – 297

3

Helix

306 – 312

7

Beta strand

318 – 321

4

Helix

328 – 330

3

Helix

334 – 344

11

Beta strand

350 – 353

4

Helix

381 – 398

18

Helix

403 – 408

6

Beta strand

410 – 419

10

Helix

433 – 436

4

Turn

442 – 444

3

Helix

448 – 454

7

Beta strand

455 – 458

4

Helix

459 – 466

8

Beta strand

472 – 474

3

Helix

476 – 478

3

Beta strand

480 – 486

7

Beta strand

491 – 501

11

Turn

505 – 508

4

Beta strand

510 – 521

12

Beta strand

525 – 538

14

Helix

541 – 548

8

Beta strand

553 – 557

5

Helix

565 – 578

14

Helix

582 – 591

10

Turn

592 – 594

3

Helix

596 – 608

13

Helix

614 – 617

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 338872AADA789FBF	FASTA	619	70,182
	10 20 30 40 50 60 MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS RLEEDDGDVA 70 80 90 100 110 120 MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR APPERGGAGT SQDGTSKNWF 130 140 150 160 170 180 KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI EFHYENTRAQ FFVEDASTAS ALKAVNYKIL 190 200 210 220 230 240 DRENRRISII INSSAPPHTI LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA 250 260 270 280 290 300 QNIDVVLNRR SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG 310 320 330 340 350 360 NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYISA IRERFPKLLR LDGHELPPPI 370 380 390 400 410 420 AFDVEAPTTL PPCKGSYFGT ENLKSLVLHF LQQYYAIYDS GDRQGLLDAY HDGACCSLSI 430 440 450 460 470 480 PFIPQNPARS SLAEYFKDSR NVKKLKDPTL RFRLLKHTRL NVVAFLNELP KTQHDVNSFV 490 500 510 520 530 540 VDISAQTSTL LCFSVNGVFK EVDGKSRDSL RAFTRTFIAV PASNSGLCIV NDELFVRNAS 550 560 570 580 590 600 SEEIQRAFAM PAPTPSSSPV PTLSPEQQEM LQAFSTQSGM NLEWSQKCLQ DNNWDYTRSA 610 QAFTHLKAKG EIPEVAFMK
	Isoform 2 [UniParc]. Checksum: 470701F5324EC0B5	FASTA	356	40,476
	10 20 30 40 50 60 MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS RLEEDDGDVA 70 80 90 100 110 120 MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR APPERGGAGT SQDGTSKNWF 130 140 150 160 170 180 KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI EFHYENTRAQ FFVEDASTAS ALKAVNYKIL 190 200 210 220 230 240 DRENRRISII INSSAPPHTI LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA 250 260 270 280 290 300 QNIDVVLNRR SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG 310 320 330 340 350 NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYIRS VVACVSPPGD LHPLGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus." Braun I.C., Rohrbach E., Schmitt C., Izaurralde E. EMBO J. 18:1953-1965(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS. Tissue: Cervix carcinoma.
[2]	"The human Tap protein is a nuclear mRNA export factor that contains novel RNA-binding and nucleocytoplasmic transport sequences." Kang Y., Cullen B.R. Genes Dev. 13:1126-1139(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirus mRNAs." Bear J., Tan W., Zolotukhin A.S., Tabernero C., Hudson E.A., Felber B.K. Mol. Cell. Biol. 19:6306-6317(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Lung and Trachea.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Placenta.
[8]	"Tap: a novel cellular protein that interacts with tip of herpesvirus saimiri and induces lymphocyte aggregation." Yoon D.-W., Lee H., Seol W., DeMaria M., Rosenzweig M., Jung J.U. Immunity 6:571-582(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-619, INTERACTION WITH SAIMIRIINE HERPESVIRUS 2 TIP. Tissue: Lymphocyte.
[9]	"TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus." Grueter P., Tabernero C., von Kobbe C., Schmitt C., Saavedra C., Bachi A., Wilm M., Felber B.K., Izaurralde E. Mol. Cell 1:649-659(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human." Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U., Hurt E. EMBO J. 18:2593-2609(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NUPL2.
[11]	"Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export." Braun I.C., Herold A., Rode M., Conti E., Izaurralde E. J. Biol. Chem. 276:20536-20543(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[12]	"The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates." Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C., Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E. RNA 6:136-158(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[13]	"Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins." Suyama M., Doerks T., Braun I.C., Sattler M., Izaurralde E., Bork P. EMBO Rep. 1:53-58(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[14]	"Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex." Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G. EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
[15]	"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex." Kim V.N., Kataoka N., Dreyfuss G. Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
[16]	"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1." Lykke-Andersen J., Shu M.-D., Steitz J.A. Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH RBM8A; UPF1; UPF2; UPF3A; UPF3B AND RNPS1.
[17]	"eIF4A3 is a novel component of the exon junction complex." Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G. RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF4A3 AND ALYREF/THOC4.
[18]	"UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA." Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T., Jones R., Ponting C.P., Dickman M.J., Wilson S.A. Curr. Biol. 19:1918-1924(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FYTTD1.
[19]	"Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA." Katahira J., Inoue H., Hurt E., Yoneda Y. EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ALYREF/THOC4 AND THOC5.
[20]	"Assembly and mobility of exon-exon junction complexes in living cells." Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M. RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[21]	"The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable." Johnson L.A., Li L., Sandri-Goldin R.M. J. Virol. 83:6335-6346(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN HERPES VIRUS 1 ICP27.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain." Liker E., Fernandez E., Izaurralde E., Conti E. EMBO J. 19:5587-5598(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 102-372.
[24]	"Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor." Fribourg S., Braun I.C., Izaurralde E., Conti E. Mol. Cell 8:645-656(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NXT1, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NXT1-FG-REPEAT, SUBUNIT, DOMAINS, MUTAGENESIS OF LEU-383; LEU-386; ASP-399; ASP-482; ILE-518; PRO-521 AND TRP-594.
[25]	"Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution." Grant R.P., Neuhaus D., Stewart M. J. Mol. Biol. 326:849-858(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 561-619 IN COMPLEX WITH RANBP3.
[26]	"Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1." Grant R.P., Hurt E., Neuhaus D., Stewart M. Nat. Struct. Biol. 9:247-251(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 551-619, MUTAGENESIS OF PHE-617.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ132712 mRNA. Translation: CAA10753.1.
AF112880 mRNA. Translation: AAD39102.1.
AF126246 mRNA. Translation: AAD20016.1.
AK304137 mRNA. Translation: BAG65031.1.
AK027192 mRNA. No translation available.
AP001160 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74105.1.
BC004904 mRNA. Translation: AAH04904.1.
BC028041 mRNA. Translation: AAH28041.1.
U80073 mRNA. Translation: AAB81111.1.

IPI

IPI00033153.
IPI00749024.

RefSeq

NP_001074960.1. NM_001081491.1.
NP_006353.2. NM_006362.4.

UniGene

Hs.523739.
Hs.601546.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FO1	X-ray	2.90	A/B	102-372	[»]
1FT8	X-ray	3.15	A/B/C/D/E	102-372	[»]
1GO5	NMR	-	A	551-619	[»]
1JKG	X-ray	1.90	B	371-619	[»]
1JN5	X-ray	2.80	B	371-619	[»]
1KOH	X-ray	3.80	A/B/C/D	96-372	[»]
1KOO	X-ray	3.80	A/B/C/D	96-372	[»]
1OAI	X-ray	1.00	A	561-619	[»]
2Z5K	X-ray	2.60	B	53-82	[»]
2Z5M	X-ray	3.00	B	53-82	[»]
3RW6	X-ray	2.30	A/B	96-362	[»]
3RW7	X-ray	3.00	A/B/C/D	96-362	[»]

ProteinModelPortal

Q9UBU9.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UBU9. 47 interactions.

MINT

MINT-121360.

STRING

9606.ENSP00000294172.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

Q9UBU9.

Polymorphism databases

DMDM

20139282.

Proteomic databases

PaxDb

Q9UBU9.

PeptideAtlas

Q9UBU9.

PRIDE

Q9UBU9.

Protocols and materials databases

DNASU

10482.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000294172; ENSP00000294172; ENSG00000162231.
ENST00000439713; ENSP00000408864; ENSG00000162231.
ENST00000531709; ENSP00000453885; ENSG00000162231.
ENST00000532297; ENSP00000436679; ENSG00000162231.

GeneID

10482.

KEGG

hsa:10482.

UCSC

uc001nvf.1. human.
uc001nvg.1. human.

Organism-specific databases

CTD

10482.

GeneCards

GC11M062559.

HGNC

HGNC:8071. NXF1.

HPA

CAB016327.

MIM

602647. gene.

neXtProt

NX_Q9UBU9.

PharmGKB

PA31858.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG324438.

HOGENOM

HOG000236269.

HOVERGEN

HBG013199.

InParanoid

Q9UBU9.

KO

K14284.

OMA

RKYDKSW.

OrthoDB

EOG4PK27D.

PhylomeDB

Q9UBU9.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9UBU9.

Bgee

Q9UBU9.

CleanEx

HS_NXF1.

Genevestigator

Q9UBU9.

GermOnline

ENSG00000162231. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR001611. Leu-rich_rpt.
IPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR005637. TAP_C_dom.
IPR015245. Tap_RNA-bd.
IPR003603. U2A'_phosphoprotein32A_C.
IPR009060. UBA-like.
[Graphical view]

Pfam

PF00560. LRR_1. 1 hit.
PF02136. NTF2. 1 hit.
PF09162. Tap-RNA_bind. 1 hit.
PF03943. TAP_C. 1 hit.
[Graphical view]

ProDom

PD043466. Tap_RNA_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00446. LRRcap. 1 hit.
SM00804. TAP_C. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS51450. LRR. 3 hits.
PS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. False negative.
PS51281. TAP_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NXF1. human.

EvolutionaryTrace

Q9UBU9.

GenomeRNAi

10482.

NextBio

39766.

SOURCE

Search...

Entry information

Entry name

NXF1_HUMAN

Accession

Primary (citable) accession number: Q9UBU9
Secondary accession number(s): B4E269, Q99799, Q9UQL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.